A strategy is described for computing the three-dimensional structure of globular proteins from the amino acid sequence alone. Earlier computational approaches have been hindered by the inherent computational complexity of this problem. Our strategy will benefit from two important constraints on the computation, both taken from our own recent results in this area. Our work showing the existence of hierarchies of domains in globular proteins indicates that any folding pathway leading to the native state must be consistent with a hierarchical mechanism of self-assembly. Our work on peptide chain turns shows that interacting chain segments forming the hydrophobic core can be successfully predicted. Taken together, these results lend themselves to a generation and screening algorithm that should yield a set of trial solutions small enough to be exhaustively considered. Such a strategy assures new chemical insight into the folding problem because it utilizes intrinsic modules, similar to the ones that can be recognized in x-ray elucidated proteins. It is also our goal here to use these techniques to characterize the shape and energetics at domain interfaces and use this data to systematically examine cofactor binding in enzymes. A control experiment that compares the chain entropy of domain hierarchies in biological proteins with that of randomly generated chains is also presented.